SPC50120
SP Sephadex® C-50 sodium form
Synonym(s):
Sulfopropyl Sephadex®
Sign Into View Organizational & Contract Pricing
All Photos(2)
About This Item
Recommended Products
bead size
40-125 μm (dry)
Quality Level
pore size
200,000 exclusion limit (av. mol. wt.)
operating pH
2-10
capacity
2.0-2.8 meq/g ion exchange capacity
2.0-2.8 meq/g
compatibility
mode of use strong cation exchange chromatography
Application
SP Sephadex® is used in protein chromatography, ion exchange chromatography and cation exchange media. SP Sephadex® has been used to study human tumors as well as to discuss the biochemical basis for the use of mebendazole in the treatment of echinococcosis.
Legal Information
Sephadex is a registered trademark of Cytiva
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
J B Starren et al.
Cellular immunology, 104(1), 59-70 (1987-01-01)
We have examined the isotypic pattern of the response of mice to the Ir gene-controlled antigen, dinitrophenyl-ovomucoid (DNP-OM). H-2 kappa mice are high responders (HR); (H-2b,d mice are low responders (LR). The isotype patterns of HR and LR strains differ
B G Wallace
The Journal of neuroscience : the official journal of the Society for Neuroscience, 10(11), 3576-3582 (1990-11-01)
Heparin and heparan sulfate have been shown to block nerve-induced acetylcholine-receptor (AChR) aggregation at developing neuromuscular junctions. We found that heparin, heparan sulfate, and a wide variety of other polyanions also inhibited agrin-induced AChR aggregation. The more highly charged the
A convenient large scale preparation of the EE isozyme of horse liver alcohol dehydrogenase.
D C Anderson et al.
Analytical biochemistry, 99(2), 392-398 (1979-11-01)
Isolation and partial characterization of a porcine thyroglobulin-binding <I>Phaseolus vulgaris</I> L. lectin.
Bonorden, W.R., and Swanson, B.G.
Food Chemistry, 44(3), 227-233 (1992)
Partial purification and kinetic properties of cytoplasmic malate dehydrogenase from ovine liver Echinococcus granulosus protoscolices
Vessal, M. and Tabei, S.M.
Comp. Biochem. Physiol., B: Comp. Biochem., 113, 757-763 (1996)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service